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dc.contributor.authorShelton, Catherine L.
dc.contributor.authorMeneely, Kathleen M.
dc.contributor.authorRonnebaum, Trey A.
dc.contributor.authorChilton, Annemarie S.
dc.contributor.authorRiley, Andrew P.
dc.contributor.authorPrisinzano, Thomas E.
dc.contributor.authorLamb, Audrey L.
dc.date.accessioned2023-02-28T15:30:02Z
dc.date.available2023-02-28T15:30:02Z
dc.date.issued2022-05-05
dc.identifier.citationShelton, C.L., Meneely, K.M., Ronnebaum, T.A. et al. Rational inhibitor design for Pseudomonas aeruginosa salicylate adenylation enzyme PchD. J Biol Inorg Chem 27, 541–551 (2022). https://doi.org/10.1007/s00775-022-01941-8en_US
dc.identifier.urihttp://hdl.handle.net/1808/33962
dc.description.abstractPseudomonas aeruginosa is an increasingly antibiotic-resistant pathogen that causes severe lung infections, burn wound infections, and diabetic foot infections. P. aeruginosa produces the siderophore pyochelin through the use of a non-ribosomal peptide synthetase (NRPS) biosynthetic pathway. Targeting members of siderophore NRPS proteins is one avenue currently under investigation for the development of new antibiotics against antibiotic-resistant organisms. Here, the crystal structure of the pyochelin adenylation domain PchD is reported. The structure was solved to 2.11 Å when co-crystallized with the adenylation inhibitor 5′-O-(N-salicylsulfamoyl)adenosine (salicyl-AMS) and to 1.69 Å with a modified version of salicyl-AMS designed to target an active site cysteine (4-cyano-salicyl-AMS). In the structures, PchD adopts the adenylation conformation, similar to that reported for AB3403 from Acinetobacter baumannii.en_US
dc.publisherSpringeren_US
dc.rights© The Author(s) 2022. This article is licensed under a Creative Commons Attribution 4.0 International License.en_US
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/en_US
dc.subjectAdenylation domainen_US
dc.subjectPseudomonas aeruginosaen_US
dc.subjectInhibitor designen_US
dc.subjectAntibiotic resistanceen_US
dc.subjectPyochelinen_US
dc.titleRational inhibitor design for Pseudomonas aeruginosa salicylate adenylation enzyme PchDen_US
dc.typeArticleen_US
kusw.kuauthorShelton, Catherine L.
kusw.kuauthorMeneely, Kathleen M.
kusw.kuauthorRonnebaum, Trey A.
kusw.kuauthorChilton, Annemarie S.
kusw.kuauthorRiley, Andrew P.
kusw.kuauthorPrisinzano, Thomas E.
kusw.kuauthorLamb, Audrey L.
kusw.kudepartmentMolecular Biosciencesen_US
kusw.kudepartmentMedicinal Chemistryen_US
dc.identifier.doi10.1007/s00775-022-01941-8en_US
dc.identifier.orcidhttps://orcid.org/0000-0002-2352-2130en_US
kusw.oaversionScholarly/refereed, publisher versionen_US
kusw.oapolicyThis item meets KU Open Access policy criteria.en_US
dc.identifier.pmidPMC9470617en_US
dc.rights.accessrightsopenAccessen_US


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© The Author(s) 2022. This article is licensed under a Creative Commons Attribution 4.0 International License.
Except where otherwise noted, this item's license is described as: © The Author(s) 2022. This article is licensed under a Creative Commons Attribution 4.0 International License.